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关于内在无序蛋白质的专题小型综述系列介绍。

Introduction to the Thematic Minireview Series on Intrinsically Disordered Proteins.

作者信息

Banerjee Ruma

机构信息

From the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600

出版信息

J Biol Chem. 2016 Mar 25;291(13):6679-80. doi: 10.1074/jbc.R116.719930. Epub 2016 Feb 5.

Abstract

In this thematic minireview series, the JBC presents six exciting articles on low complexity or intrinsically disordered proteins (IDPs). The dynamical and fluctuating structures of IDPs or of disordered regions within proteins result in virtually all of their primary sequence being exposed, at least at some time, to potential interacting partners. Their structural versatility underlies their often wide functional repertoires, which is further expanded by post-translational modifications. Given these characteristics, it is not surprising that IDPs serve as important hubs in signaling networks, scaffolding multivalent interactions. They are also important for organizing membrane-less protein organelles. This collection of reviews discusses biophysical approaches for studying IDPs and illuminates their importance to critical functions such as cell cycle control, transcription, and translation, as well as their regulation via cellular input signals.

摘要

在这个主题迷你综述系列中,《生物化学杂志》(JBC)发表了六篇关于低复杂性或内在无序蛋白质(IDP)的精彩文章。IDP或蛋白质内无序区域的动态和波动结构导致其几乎所有一级序列至少在某些时候都暴露于潜在的相互作用伙伴。它们的结构多功能性是其通常广泛的功能库的基础,翻译后修饰进一步扩展了这些功能库。鉴于这些特性,IDP作为信号网络中的重要枢纽,介导多价相互作用,也就不足为奇了。它们对于组织无膜蛋白质细胞器也很重要。这组综述讨论了研究IDP的生物物理方法,并阐明了它们对细胞周期控制、转录和翻译等关键功能的重要性,以及它们通过细胞输入信号进行的调节。

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本文引用的文献

1
Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins.
J Biol Chem. 2016 Mar 25;291(13):6681-8. doi: 10.1074/jbc.R115.685859. Epub 2016 Feb 5.
2
Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.
J Biol Chem. 2016 Mar 25;291(13):6706-13. doi: 10.1074/jbc.R115.692590. Epub 2016 Feb 5.
3
Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.
J Biol Chem. 2016 Mar 25;291(13):6696-705. doi: 10.1074/jbc.R115.695056. Epub 2016 Feb 5.
6
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.
J Biol Chem. 2016 Mar 25;291(13):6689-95. doi: 10.1074/jbc.R115.692715. Epub 2016 Feb 5.

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